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(ET)-1 is a peptide isolated from the culture medium of porcine aortic cells whose mRNA is widely expressed in human endothelial cells (20). Three distinct isoforms, ET-l, ET-2, ET-3, have been identified. Endothelin synthesis is not limited to the vascular endothelium; other types of cells, including those of the lung, kidney, gut, can synthesize endothelin (8, 10, 18). Abundant expression of ET-l peptide the mRNA of its precursor, prepro-ET-l, have been found not only in the vascular endothelium of the renal vascular bed, including the glomerular capillaries arterioles the peritubular capillaries (10, 12, 13), but also in high concentration in the inner medullary collecting duct (8). The biological activities of the endothelins are mediated by at least two distinct endothelin receptors, designated ETA ETB (20), which are widely distributed in a number of tissues, most notably the vascular wall, heart, lung, kidney (20). ET* is highly sensitive to ET-1 ET-2, but all three endothelin isopeptides have equal finity for ET B. ETA, which is found on smooth muscle cells, mediates constriction, whereas ETB is found on endothelial cells mediates the production of endothelium-derived relaxing factor (20). ENDOTHELIN 0363-6135/95 $3.00 Copyright 0 1995 Early characterization studies of ET-1 revealed
AJP - Heart and Circulatory Physiology – The American Physiological Society
Published: May 1, 1995
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